Vibrational analysis of peptides, polypeptides, and proteins. VI. Assignment of β-turn modes in insulin and other proteins

✍ Scribed by Jagdeesh Bandekar; S. Krimm

• Publisher: Wiley (John Wiley & Sons)
• Year: 1980
• Tongue: English
• Weight: 343 KB
• Volume: 19
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1980.360190103

✦ Synopsis

Abstract

The normal modes have been calculated for structures having the dihedral angles of the four β‐turns of insulin. Frequencies are predicted in the amide I region near 1652 and 1680 cm^−1^. The former overlaps the α‐helix band at 1658 cm^−1^ in the Raman spectrum, while the latter accounts for the hitherto unassignable band at 1681 cm^−1^. Calculated amide III frequencies extend above 1300 cm^−1^, providing a compelling assignment of the 1303‐cm^−1^ band in insulin and similar bands in other globular proteins.